Cargando…

A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells

Peptides and proteins can convert from their soluble forms into highly ordered fibrillar aggregates, giving rise to pathological conditions ranging from neurodegenerative disorders to systemic amyloidoses. It is increasingly recognized that protein oligomers forming early in the process of fibril ag...

Descripción completa

Detalles Bibliográficos
Autores principales:	Zampagni, Mariagioia, Cascella, Roberta, Casamenti, Fiorella, Grossi, Cristina, Evangelisti, Elisa, Wright, Daniel, Becatti, Matteo, Liguri, Gianfranco, Mannini, Benedetta, Campioni, Silvia, Chiti, Fabrizio, Cecchi, Cristina
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Blackwell Publishing Ltd 2011
Materias:	Articles
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4394221/ https://www.ncbi.nlm.nih.gov/pubmed/21155974 http://dx.doi.org/10.1111/j.1582-4934.2010.01239.x

Ejemplares similares

Chaperones as Suppressors of Protein Misfolded Oligomer Toxicity
por: Mannini, Benedetta, et al.
Publicado: (2017)

Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases
por: Evangelisti, Elisa, et al.
Publicado: (2016)

Effects of oligomer toxicity, fibril toxicity and fibril spreading in synucleinopathies
por: Cascella, Roberta, et al.
Publicado: (2022)

Aβ Oligomers Dysregulate Calcium Homeostasis by Mechanosensitive Activation of AMPA and NMDA Receptors
por: Fani, Giulia, et al.
Publicado: (2021)

Interaction of toxic and non-toxic HypF-N oligomers with lipid bilayers investigated at high resolution with atomic force microscopy
por: Oropesa-Nuñez, Reinier, et al.
Publicado: (2016)

Characterization of Pairs of Toxic and Nontoxic Misfolded Protein Oligomers Elucidates the Structural Determinants of Oligomer Toxicity in Protein Misfolding Diseases
por: Limbocker, Ryan, et al.
Publicado: (2023)

Large Proteins Have a Great Tendency to Aggregate but a Low Propensity to Form Amyloid Fibrils
por: Ramshini, Hassan, et al.
Publicado: (2011)

The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells
por: Cascella, Roberta, et al.
Publicado: (2021)

Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers
por: Limbocker, Ryan, et al.
Publicado: (2021)

Therapeutic Strategies to Reduce the Toxicity of Misfolded Protein Oligomers
por: Kreiser, Ryan P., et al.
Publicado: (2020)

Exploring the Release of Toxic Oligomers from α-Synuclein Fibrils with Antibodies and STED Microscopy
por: Bigi, Alessandra, et al.
Publicado: (2021)

Trodusquemine enhances Aβ(42) aggregation but suppresses its toxicity by displacing oligomers from cell membranes
por: Limbocker, Ryan, et al.
Publicado: (2019)

Rationally Designed Antibodies as Research Tools to Study the Structure–Toxicity Relationship of Amyloid-β Oligomers
por: Limbocker, Ryan, et al.
Publicado: (2020)

Misfolded protein oligomers induce an increase of intracellular Ca(2+) causing an escalation of reactive oxidative species
por: Fani, Giulia, et al.
Publicado: (2022)

Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers
por: Patel, Jayneil R., et al.
Publicado: (2018)

A quantitative biology approach correlates neuronal toxicity with the largest inclusions of TDP-43
por: Cascella, Roberta, et al.
Publicado: (2022)

Probing the Origin of the Toxicity of Oligomeric Aggregates of α-Synuclein with Antibodies
por: Cascella, Roberta, et al.
Publicado: (2019)

Distinct responses of human peripheral blood cells to different misfolded protein oligomers
por: Leal‐Lasarte, Magdalena, et al.
Publicado: (2021)

Transthyretin Inhibits Primary and Secondary Nucleations of Amyloid-β Peptide Aggregation and Reduces the Toxicity of Its Oligomers
por: Ghadami, Seyyed Abolghasem, et al.
Publicado: (2020)

Sphingosine 1‐phosphate attenuates neuronal dysfunction induced by amyloid‐β oligomers through endocytic internalization of NMDA receptors
por: Bigi, Alessandra, et al.
Publicado: (2022)

α-Synuclein oligomers and fibrils: partners in crime in synucleinopathies
por: Bigi, Alessandra, et al.
Publicado: (2023)

TDP-43 Inclusion Bodies Formed in Bacteria Are Structurally Amorphous, Non-Amyloid and Inherently Toxic to Neuroblastoma Cells
por: Capitini, Claudia, et al.
Publicado: (2014)

The Toxicity of Protein Aggregates: New Insights into the Mechanisms
por: Bigi, Alessandra, et al.
Publicado: (2023)

Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans
por: Perni, Michele, et al.
Publicado: (2021)

Toxic oligomers of the amyloidogenic HypF-N protein form pores in mitochondrial membranes
por: Farrugia, Maria Ylenia, et al.
Publicado: (2020)

Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism
por: Limbocker, Ryan, et al.
Publicado: (2020)

Destabilisation, aggregation, toxicity and cytosolic mislocalisation of nucleophosmin regions associated with acute myeloid leukemia
por: Scognamiglio, Pasqualina Liana, et al.
Publicado: (2016)

Probing the Structure of Toxic Amyloid-β Oligomers with Electron Spin Resonance and Molecular Modeling
por: Banchelli, Martina, et al.
Publicado: (2021)

The Toxicity of Amyloid β Oligomers
por: Zhao, Li Na, et al.
Publicado: (2012)

Soluble Prion Peptide 107–120 Protects Neuroblastoma SH-SY5Y Cells against Oligomers Associated with Alzheimer’s Disease
por: Rezvani Boroujeni, Elham, et al.
Publicado: (2020)

Nanoscopic insights into the surface conformation of neurotoxic amyloid β oligomers
por: Banchelli, Martina, et al.
Publicado: (2020)

The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity
por: Xu, Catherine K., et al.
Publicado: (2022)

Lithium Improves Hippocampal Neurogenesis, Neuropathology and Cognitive Functions in APP Mutant Mice
por: Fiorentini, Anna, et al.
Publicado: (2010)

Partial Failure of Proteostasis Systems Counteracting TDP-43 Aggregates in Neurodegenerative Diseases
por: Cascella, Roberta, et al.
Publicado: (2019)

The Toxicity and Polymorphism of β-Amyloid Oligomers
por: Huang, Ya-ru, et al.
Publicado: (2020)

Structural Features and Toxicity of α-Synuclein Oligomers Grown in the Presence of DOPAC
por: Palazzi, Luana, et al.
Publicado: (2021)

Quantitative Measurement of the Affinity of Toxic and Nontoxic Misfolded Protein Oligomers for Lipid Bilayers and of its Modulation by Lipid Composition and Trodusquemine
por: Errico, Silvia, et al.
Publicado: (2021)

Shared amyloid oligomer structure proves toxic
por: Tuma, Rabiya S.
Publicado: (2003)

Membrane Interactions and Toxicity by Misfolded Protein Oligomers
por: Gonzalez-Garcia, Mario, et al.
Publicado: (2021)

Formation and Toxicity of Soluble Polyglutamine Oligomers in Living Cells
por: Lajoie, Patrick, et al.
Publicado: (2010)

Cannot write session to /tmp/vufind_sessions/sess_ohuja7c1tkm8mg7p5nsoafpckn